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Physicochemical studies of caroubin: a gluten-like protein.

Authors
  • Wang, Y
  • Belton, P S
  • Bridon, H
  • Garanger, E
  • Wellner, N
  • Parker, M L
  • Grant, A
  • Feillet, P
  • Noel, T R
Type
Published Article
Journal
Journal of agricultural and food chemistry
Publication Date
Jul 01, 2001
Volume
49
Issue
7
Pages
3414–3419
Identifiers
PMID: 11453784
Source
Medline
License
Unknown

Abstract

It has been reported that caroubin, a protein mixture obtained from carob seeds, has rheological properties similar to those of gluten. Comparative studies of the effects of hydration and temperature on caroubin and gluten were carried out with the aid of NMR, FTIR, scanning electron microscopy, and differential scanning calorimetry techniques. The results show that caroubin has a more ordered structure than gluten and that hydration has little effect on its secondary structure when compared to gluten. Caroubin is more easily accessible to water than gluten, suggesting that caroubin is more hydrophilic in nature. On hydration, caroubin, like gluten, forms fibrillar structures and sheets.

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